منابع مشابه
Phosphorylation of Titin Modulates Passive Stiffness of Cardiac Muscle in a Titin Isoform-dependent Manner
We investigated the effect of protein kinase A (PKA) on passive force in skinned cardiac tissues that express different isoforms of titin, i.e., stiff (N2B) and more compliant (N2BA) titins, at different levels. We used rat ventricular (RV), bovine left ventricular (BLV), and bovine left atrial (BLA) muscles (passive force: RV > BLV > BLA, with the ratio of N2B to N2BA titin, approximately 90:1...
متن کاملPhosphorylation of titin modulates pas- sive stiffness of cardiac muscle in a titin
Question: How does phosphorylation of titan affect cardiac function? Background: Sarcomeres are the repeating contractile subunits from which the myofibrils of striated muscle are built. Titin is a large sarcomeric protein involved in muscle elasticity and myofibril scaffolding, which provides passive tension to muscle based on physiological demands. In mammalian cardiac tissue, there are two i...
متن کاملAcute exercise modifies titin phosphorylation and increases cardiac myofilament stiffness
Titin-based myofilament stiffness is largely modulated by phosphorylation of its elastic I-band regions N2-Bus (decreases passive stiffness, PT) and PEVK (increases PT). Here, we tested the hypothesis that acute exercise changes titin phosphorylation and modifies myofilament stiffness. Adult rats were exercised on a treadmill for 15 min, untrained animals served as controls. Titin phosphorylati...
متن کاملProtein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs
The sarcomeric titin springs influence myocardial distensibility and passive stiffness. Titin isoform composition and protein kinase (PK)A-dependent titin phosphorylation are variables contributing to diastolic heart function. However, diastolic tone, relaxation speed, and left ventricular extensibility are also altered by PKG activation. We used back-phosphorylation assays to determine whether...
متن کاملD-Titin
Previously, we reported that chromosomes contain a giant filamentous protein, which we identified as titin, a component of muscle sarcomeres. Here, we report the sequence of the entire titin gene in Drosophila melanogaster, D-Titin, and show that it encodes a two-megadalton protein with significant colinear homology to the NH(2)-terminal half of vertebrate titin. Mutations in D-Titin cause chro...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Circulation Research
سال: 2009
ISSN: 0009-7330,1524-4571
DOI: 10.1161/circresaha.109.206912